ID A0A218KC22_9CAUD Unreviewed; 652 AA.
AC A0A218KC22;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=PBC2_125 {ECO:0000313|EMBL:AKQ08440.1};
OS Bacillus phage PBC2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=1675029 {ECO:0000313|EMBL:AKQ08440.1, ECO:0000313|Proteomes:UP000223102};
RN [1] {ECO:0000313|EMBL:AKQ08440.1, ECO:0000313|Proteomes:UP000223102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kong M., Ryu S.;
RT "Complete genome sequence of Bacillus cereus phage PBC2.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; KT070867; AKQ08440.1; -; Genomic_DNA.
DR Proteomes; UP000223102; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd01030; TOPRIM_TopoIIA_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AKQ08440.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000223102};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 428..551
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 652 AA; 74413 MW; 6A46D4C54C77D3BA CRC64;
MSDNIRQLSE KEKVRKKISV WLGASNHIAV LHTIKEIIGN SADEINKGRG DEIRIVRHTD
KRITIVDNCQ GLPLEGKNSD GVDNYKLLFE TLFAGTKYEN GISNNDYTVG VNGVFNTVLT
FSSKDVTFEV ARPDGNIYSI SYHKGENISP LRVIGKSSKT YTKITYELDD DIFEENYFDV
AELSEIASQQ ASLIKGAVIV KDEVLNTEDV FEFKNGIVDF LDGETKSLTD LHDMIVFQKD
ISHELKQEGK DVTDDIKISI AMKYTKEDDK TTQIEFLNGS NLIHHGTIYD GLVAGLRNIV
NRYLKDNNMY KKDEKQITKE DVIVGLNYVI DFKSYFPVFA NQTKFASYVK YYEEVMKSAL
ESFFESYIVE RKNDMNLIAK QILITKQSRE KAEKTRLDFK KKLSGTVNNL TARVDGFVSC
TSKDKSITEF YIVEGKSALG STQQGRDPLF QAIYALRGKT LNCLKADYDK IFKNDIIVDL
IKILGCGVEV KSKHAKDLNT FDIENLRWSK VIIATDADVD GFHIRTLILT MIYRLMPTLI
EEGYIYIAES PLYEITQNDV SVFAYNDAEK DEIVSKMTGS YTIQRSKGLG ENTAEMMWDT
TMNPETRRLI QIKPDDFEET MKTFELFLGD NLEGRKEYIE NNLHKYVEDV LD
//
